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2 results on '"J.P. Muh"'

1. Purification and characterization of ubiquitin from mammalian testis

Author

J.P. Muh, Pierre Sautiere, Yves Menezo, Maurice Loir, A. Caraty, and M. Lanneau

Subjects
Male, Gel filtration chromatography, Chromosomal Proteins, Non-Histone, Protein Conformation, Size-exclusion chromatography, Radioimmunoassay, Biophysics, Biology, Biochemistry, Protein structure, Ubiquitin, Structural Biology, Testis, Genetics, Animals, Amino Acid Sequence, Amino Acids, Ubiquitins, Molecular Biology, Peptide sequence, Mammals, chemistry.chemical_classification, Mammalian testis, Cell Biology, Molecular biology, Nucleoprotein, Amino acid, Nucleoproteins, chemistry, Chromatography, Gel, biology.protein, Oxidation-Reduction, Amino acid analysis
Abstract

Ubiquitin was extracted from testis of 4 mammals and purified to homogeneity by gel filtration chromatography. Amino acid compositions and NH2-terminal sequences were found to be identical in the 4 species and with calf thymus ubiquitin. Ubiquitin conformation was shown to be very sensitive to oxidation. Improved methods for radioimmunoassay of ubiquitin in tissue extracts are also discussed.

Published
1984

2. Distribution of non-enzymatically bound glucose in in vivo and in vitro glycosylated type I collagen molecules

Author

J.D. Guitton, Alain Le Pape, and J.P. Muh

Subjects
Male, Glycosylation, Biophysics, Peptide, Cleavage (embryo), Biochemistry, chemistry.chemical_compound, Structural Biology, Glycation, In vivo, Genetics, Animals, Fluorometry, Cyanogen Bromide, Molecular Biology, Fluorography, chemistry.chemical_classification, Chemistry, Diabetes, Nonenzymatic glycosylation, Fibrillogenesis, Rats, Inbred Strains, Cell Biology, In vitro, Peptide Fragments, Rats, carbohydrates (lipids), Glucose, CNBr cleavage, Electrophoresis, Polyacrylamide Gel, Collagen, Glucose localization, Type I collagen
Abstract

Non-enzymatic glycosylation of collagen occurs both in vivo during diabetes and in vitro after incubation with glucose. Glycosylated collagen exhibits altered physicochemical and biological properties which could explain some of the complications of diabetes. To provide a mechanistic explanation of this modification the localization of bound glucose was investigated using NaB[3H]H4 reduction and CNBr cleavage. Glucose fixation is distributed mainly on the alpha 1CB6 peptide after in vitro glycosylation whereas this distribution occurs less specifically during diabetes. It is concluded that fibrillogenesis alteration of in vitro glycosylated collagen is related to glucose fixation on free epsilon NH2 sites normally implied in intermolecular interactions.

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